Journal of Bioscience and Bioengineering Vol. 103, No. 5 (2007)
Vol. 103, May 2007
Superimposition of structures of amylomaltase.
The structure of Thermus aquaticus amylomaltase in native form (white) was superimposed on that in acarbose-complex form (blue). Upper panels show the overall structures and lower panels indicate the enlarged view of proposed accepter binding site. This superimposition revealed a conformational change around the acceptor binding site which is caused by the binding of substrate to the second substrate binding site 14Å away from catalytic residues.
Related article: Fujii, K., Minagawa, H., Terada, Y., Takaha, T., Kuriki, T., Shimada, J., and Kaneko, H., “Function of second glucan binding site including tyrosines 54 and 101 in Thermus aquaticus amylomaltase“, J. Biosci. Bioeng., vol. 103, 167-173 (2007).
⇒JBBアーカイブ：Vol.107 (2009) ～最新号
⇒JBBアーカイブ：Vol. 93（2002）～Vol. 106（2008）
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